| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 7755415 | Journal of Inorganic Biochemistry | 2012 | 10 Pages |
Abstract
⺠Catalase-negative KatGs were made by Y226F exchange and LL1 deletion and compared. ⺠Deletion produced up to ten-fold greater peroxidase activity than substitution. ⺠Deletion variants were also much less sensitive to H2O2-dependent inactivation. ⺠Both types of variants showed similar kinetics of compound I, II, and III formation. ⺠Deletion gave 60 fold more rapid ferryl intermediate reduction by electron donors.
Related Topics
Physical Sciences and Engineering
Chemistry
Inorganic Chemistry
Authors
Shalley N. Kudalkar, Robert A. Campbell, Yongjiang Li, Cornelius L. Varnado, Corey Prescott, Douglas C. Goodwin,